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Nanomechanical Sensing of Biological...

Du, Wenjian.

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Nanomechanical Sensing of Biological Interfacial Interactions.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Nanomechanical Sensing of Biological Interfacial Interactions./
作者:	Du, Wenjian.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2017,
面頁冊數:	181 p.
附註:	Source: Dissertation Abstracts International, Volume: 78-06(E), Section: B.
Contained By:	Dissertation Abstracts International78-06B(E).
標題:	Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10254334
ISBN:	9781369515862

Nanomechanical Sensing of Biological Interfacial Interactions.
Du, Wenjian.

Nanomechanical Sensing of Biological Interfacial Interactions. - Ann Arbor : ProQuest Dissertations & Theses, 2017 - 181 p.

Source: Dissertation Abstracts International, Volume: 78-06(E), Section: B.

Thesis (Ph.D.)--Drexel University, 2017.

Cellulose is the most abundant biopolymer on earth. Cellulase is an enzyme capable of converting insoluble cellulose into soluble sugars. Cellulosic biofuel produced from such fermentable simple sugars is a promising substitute as an energy source. However, its economic feasibility is limited by the low efficiency of the enzymatic hydrolysis of cellulose by cellulase. Cellulose is insoluble and resistant to enzymatic degradation, not only because the beta-1,4-glycosidic bonds are strong covalent bonds, but also because cellulose microfibrils are packed into tightly bound, crystalline lattices. Enzymatic hydrolysis of cellulose by cellulase involves three steps---initial binding, decrystallization, and hydrolytic cleavage. Currently, the mechanism for the decrystallization has not yet been elucidated, though it is speculated to be the rate-limiting step of the overall enzymatic activity. The major technical challenge limiting the understanding of the decrystallization is the lack of an effective experimental approach capable of examining the decrystallization, an interfacial enzymatic activity on solid substrates. The work presented develops a nanomechanical sensing approach to investigate both the decrystallization and enzymatic hydrolytic cleavage of cellulose. The first experimental evidence of the decrystallization is obtained by comparing the results from native cellulase and non-hydrolytic cellulase. Surface topography has been applied to examine the activities of native cellulase and non-hydrolytic cellulase on cellulose substrate. The study demonstrates additional experimental evidence of the decrystallization in the hydrolysis of cellulose. By combining simulation and monitoring technology, the current study also investigates the structural changes of cellulose at a molecular level. In particular, the study employs cellulose nanoparticles with a bilayer structure on mica sheets. By comparing results from a molecular dynamic simulation and the distance between cellulose layers monitored by means of the atomic force microscopy (AFM), the current study shows that water molecules can efficiently reduce the energy required for separating two layers of cellulose bilayers during hydration of cellulose bilayer nanoparticles. The findings of the study contribute to explicating the mechanism of cellulose the decrystallization, a free-energetically unfavorable process, through enzymatic hydrolysis of cellulase. The study also investigates the application of a cell-based microcantilever sensor to monitor the real-time ligand-induced response of living cells. These nanomechanical approaches offer unique perspectives on the interfacial activities of biological molecules.

ISBN: 9781369515862Subjects--Topical Terms:

518028
Biochemistry.

Nanomechanical Sensing of Biological Interfacial Interactions.
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520 $a Cellulose is the most abundant biopolymer on earth. Cellulase is an enzyme capable of converting insoluble cellulose into soluble sugars. Cellulosic biofuel produced from such fermentable simple sugars is a promising substitute as an energy source. However, its economic feasibility is limited by the low efficiency of the enzymatic hydrolysis of cellulose by cellulase. Cellulose is insoluble and resistant to enzymatic degradation, not only because the beta-1,4-glycosidic bonds are strong covalent bonds, but also because cellulose microfibrils are packed into tightly bound, crystalline lattices. Enzymatic hydrolysis of cellulose by cellulase involves three steps---initial binding, decrystallization, and hydrolytic cleavage. Currently, the mechanism for the decrystallization has not yet been elucidated, though it is speculated to be the rate-limiting step of the overall enzymatic activity. The major technical challenge limiting the understanding of the decrystallization is the lack of an effective experimental approach capable of examining the decrystallization, an interfacial enzymatic activity on solid substrates. The work presented develops a nanomechanical sensing approach to investigate both the decrystallization and enzymatic hydrolytic cleavage of cellulose. The first experimental evidence of the decrystallization is obtained by comparing the results from native cellulase and non-hydrolytic cellulase. Surface topography has been applied to examine the activities of native cellulase and non-hydrolytic cellulase on cellulose substrate. The study demonstrates additional experimental evidence of the decrystallization in the hydrolysis of cellulose. By combining simulation and monitoring technology, the current study also investigates the structural changes of cellulose at a molecular level. In particular, the study employs cellulose nanoparticles with a bilayer structure on mica sheets. By comparing results from a molecular dynamic simulation and the distance between cellulose layers monitored by means of the atomic force microscopy (AFM), the current study shows that water molecules can efficiently reduce the energy required for separating two layers of cellulose bilayers during hydration of cellulose bilayer nanoparticles. The findings of the study contribute to explicating the mechanism of cellulose the decrystallization, a free-energetically unfavorable process, through enzymatic hydrolysis of cellulase. The study also investigates the application of a cell-based microcantilever sensor to monitor the real-time ligand-induced response of living cells. These nanomechanical approaches offer unique perspectives on the interfacial activities of biological molecules.
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